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The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation.

Pacienza, Natalia; Pozner, Roberto G; Bianco, Germán A; D'Atri, Lina P; Croci, Diego O; Negrotto, Soledad; Malaver, Elisa; Gómez, Ricardo M; Rabinovich, Gabriel A; Schattner, Mirta.
FASEB J ; 22(4): 1113-23, 2008 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-17984174
Platelet activation is a critical process during inflammation, thrombosis, and cancer. Here, we show that galectin-1, an endogenous lectin with immunoregulatory properties, plays a key role in human platelet activation and function. Galectin-1 binds to human platelets in a carbohydrate-dependent manner and synergizes with ADP or thrombin to induce platelet aggregation and ATP release. Furthermore, galectin-1 induces F-actin polymerization, up-regulation of P-selectin, and GPIIIa expression; promotes shedding of microvesicles; and triggers conformational changes in GPIIb/IIIa. In addition, exposure to this lectin favors the generation of leukocyte-platelet aggregates. A further mechanistic analysis revealed the involvement of Ca(2+) and cyclic nucleotide-dependent pathways in galectin-1-mediated control of platelet activation. Finally, expression of endogenous galectin-1 in human platelets contributes to ADP-induced aggregation. Our study reveals a novel unrecognized role for galectin-1 in the control of platelet physiology with potential implications in thrombosis, inflammation, and metastasis.